Bacteriocin SRCAM 602 peptide

Bacteriocin SRCAM 602 peptide

• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

H-ATYYGNGLYCNKQKHYTWVDWNKASREIGKITVNGWVQH-OH

H-Ala-Thr-Tyr-Tyr-Gly-Asn-Gly-Leu-Tyr-Cys-Asn-Lys-Gln-Lys-His-Tyr-Thr-Trp-Val-Asp-Trp-Asn-Lys-Ala-Ser-Arg-Glu-Ile-Gly-Lys-Ile-Thr-Val-Asn-Gly-Trp-Val-Gln-His-OH

39

95.23%

C₂₁₁H₃₀₇N₅₉O₅₈S

4630.1

Synthetic

Powder

Bacteriocin SRCAM 602 is a bacteriocin produced by Paenibacillus polymyxa [Bacillus polymyxa], known for its broad antimicrobial spectrum against both Gram-positive and Gram-negative bacteria.
Bacteriocin SRCAM 602 is active against various bacteria, including Campylobacter spp., which is significant for reducing Campylobacter colonization in poultry and potentially controlling this foodborne pathogen.

Normally, this peptide will be delivered in lyophilized form and should be stored in a freezer at or below -20 °C. For more details, please refer to the manual:Handling and Storage of Synthetic Peptides

• Svetoch EA, Stern NJ, Eruslanov BV, et al. Isolation of Bacillus circulans and Paenibacillus polymyxa strains inhibitory to Campylobacter jejuni and characterization of associated bacteriocins. J Food Prot. 2005;68(1):11-7.
• Lohans CT, Huang Z, van Belkum MJ, Giroud M, Sit CS, Steels EM, Zheng J, Whittal RM, McMullen LM, Vederas JC. Structural characterization of the highly cyclized lantibiotic paenicidin A via a partial desulfurization/reduction strategy. J Am Chem Soc. 2012 Dec 5;134(48):19540-3.
• Arbulu S, Jiménez JJ, Gútiez L, Cintas LM, Herranz C, Hernández PE. Cloning and expression of synthetic genes encoding the broad antimicrobial spectrum bacteriocins SRCAM 602, OR-7, E-760, and L-1077, by recombinant Pichia pastoris. Biomed Res Int. 2015;2015:767183.

Trifluoroacetic acid (TFA) has a significant impact on peptides due to its role in the peptide synthesis process.

TFA is essential for the protonation of peptides that lack basic amino acids such as Arginine (Arg), Histidine (His), and Lysine (Lys), or ones that have blocked N-termini. As a result, peptides often contain TFA salts in the final product.

TFA residues, when present in custom peptides, can cause unpredictable fluctuations in experimental data. At a nanomolar (nM) level, TFA can influence cell experiments, hindering cell growth at low concentrations (as low as 10 nM) and promoting it at higher doses (0.5–7.0 mM). It can also serve as an allosteric regulator on the GlyR of glycine receptors, thereby increasing receptor activity at lower glycine concentrations.

In an in vivo setting, TFA can trifluoroacetylate amino groups in proteins and phospholipids, inducing potentially unwanted antibody responses. Moreover, TFA can impact structure studies as it affects spectrum absorption.